ID TKT_BUCAP Reviewed; 665 AA.
AC Q8KA26;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 29-MAY-2013, entry version 77.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=BUsg_086;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC a ketose donor to an aldose acceptor, via a covalent intermediate
CC with the cofactor thiamine pyrophosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)
CC (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family.
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DR EMBL; AE013218; AAM67656.1; -; Genomic_DNA.
DR RefSeq; NP_660445.1; NC_004061.1.
DR ProteinModelPortal; Q8KA26; -.
DR SMR; Q8KA26; 4-663.
DR STRING; 198804.BUsg086; -.
DR EnsemblBacteria; AAM67656; AAM67656; BUsg_086.
DR GeneID; 1005903; -.
DR KEGG; bas:BUsg086; -.
DR PATRIC; 21246947; VBIBucAph100086_0088.
DR eggNOG; COG0021; -.
DR KO; K00615; -.
DR OMA; EFNREGH; -.
DR ProtClustDB; PRK12753; -.
DR BioCyc; BAPH198804:GHMG-95-MONOMER; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:EC.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52922; Transketo_C_like; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium; Complete proteome; Magnesium; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1 665 Transketolase.
FT /FTId=PRO_0000191854.
FT NP_BIND 114 116 Thiamine pyrophosphate (By similarity).
FT ACT_SITE 411 411 Proton donor (By similarity).
FT METAL 155 155 Magnesium (By similarity).
FT METAL 185 185 Magnesium (By similarity).
FT METAL 187 187 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 26 26 Substrate (By similarity).
FT BINDING 66 66 Thiamine pyrophosphate (By similarity).
FT BINDING 156 156 Thiamine pyrophosphate; via amide
FT nitrogen (By similarity).
FT BINDING 185 185 Thiamine pyrophosphate (By similarity).
FT BINDING 261 261 Substrate (By similarity).
FT BINDING 261 261 Thiamine pyrophosphate (By similarity).
FT BINDING 358 358 Substrate (By similarity).
FT BINDING 385 385 Substrate (By similarity).
FT BINDING 437 437 Thiamine pyrophosphate (By similarity).
FT BINDING 461 461 Substrate (By similarity).
FT BINDING 469 469 Substrate (By similarity).
FT BINDING 520 520 Substrate (By similarity).
FT SITE 26 26 Important for catalytic activity (By
FT similarity).
FT SITE 261 261 Important for catalytic activity (By
FT similarity).
SQ SEQUENCE 665 AA; 75054 MW; 650B0C0E3122115A CRC64;
MCVRRELANA IRMLSIDAVQ NAKSGHPGMP MGMADIAEVL WRKFFKHSPT NPNWNNRDRF
ILSNGHGSML LYSLLHLTGY DLSIDELKKF RQLHSKTPGH PETGETPGVE TTTGPLGQGL
ANAVGMAIAE RTLSAYFNRP DYDIVDHYTW VFVGDGCLME GISHEVCSLA GTLKLGKLIV
FYDKNGISID GKISNWFTDD TVMRFKSYNW HVVDKVDGHD ANSIKNSIEE AKSVKDQPSI
IICNTIIGFG SPNKSGTADS HGAPLGEEEI FLTRKNLNWK YSPFEIPNKI YDKWNFVKQG
LKLEENWNKQ FHLYKSEYPA LAEEYSRRIK KKLPTQWYKK TKDYIFNLQK NPQNIATRKA
SQNAIEEFAA LLPELIGGSA DLSPSNLTMW SKSSSITENL CGNYIHYGVR EFGMTAIANG
ISHHGGFIPY TSTFLMFVEY ARNAVRMAAL MNTKHIFVYT HDSIGLGEDG PTHQPIEQLA
NLRMTPNIDV WRPSDQVETA VAWKYAIEEK NGPTALILSR QNLFQFSRNN EQIKNISYGA
YILYDSKKPI DIIFISTGSE LQITLTSAKK IAALGYSVRV VSMPSNNVFD RQNIDYKESI
LPSYITKRIV IEASIKDFWY KYAGSEGLII GMETFGESAS EEVLFKKFGF TVENIVNKSK
ILLKH
//
